ID SKI8_RAT Reviewed; 305 AA.
AC Q4V7A0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 123.
DE RecName: Full=Superkiller complex protein 8;
DE Short=Ski8;
DE AltName: Full=WD repeat-containing protein 61;
DE Contains:
DE RecName: Full=Superkiller complex protein 8, N-terminally processed;
DE AltName: Full=WD repeat-containing protein 61, N-terminally processed;
GN Name=Skic8; Synonyms=Wdr61;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is implicated
CC in regulation of development and maintenance of embryonic stem cell
CC pluripotency. PAF1C associates with RNA polymerase II through
CC interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-
CC 5'-phosphorylated forms and is involved in transcriptional elongation,
CC acting both independently and synergistically with TCEA1 and in
CC cooperation with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it
CC promotes leukemogenesis through association with KMT2A/MLL1-rearranged
CC oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL.
CC PAF1C is involved in histone modifications such as ubiquitination of
CC histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C
CC recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2
CC enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C is
CC involved in mRNA 3' end formation probably through association with
CC cleavage and poly(A) factors. In case of infection by influenza A
CC strain H3N2, PAF1C associates with viral NS1 protein, thereby
CC regulating gene transcription. Required for mono- and trimethylation on
CC histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79'
CC (H3K4me3). Required for Hox gene transcription. Also acts as a
CC component of the SKI complex, a multiprotein complex that assists the
CC RNA-degrading exosome during the mRNA decay and quality-control
CC pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal
CC complexes in the 3'-5' direction and channels mRNA to the cytosolic
CC exosome for degradation. SKI-mediated extraction of mRNA from stalled
CC ribosomes allow binding of the Pelota-HBS1L complex and subsequent
CC ribosome disassembly by ABCE1 for ribosome recycling.
CC {ECO:0000250|UniProtKB:Q9GZS3}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and SKIC8 (By similarity). The PAF1 complex interacts
CC with PHF5A. Within the PAF1 complex interacts directly with PHF5A (By
CC similarity). Component of the SKI complex which consists of SKIC2,
CC SKIC3 and SKIC8 (By similarity). {ECO:0000250|UniProtKB:Q9ERF3,
CC ECO:0000250|UniProtKB:Q9GZS3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9GZS3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9GZS3}.
CC -!- SIMILARITY: Belongs to the SKI8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC098059; AAH98059.1; -; mRNA.
DR RefSeq; NP_001020914.1; NM_001025743.1.
DR RefSeq; XP_006243147.1; XM_006243085.3.
DR RefSeq; XP_006243148.1; XM_006243086.2.
DR AlphaFoldDB; Q4V7A0; -.
DR SMR; Q4V7A0; -.
DR STRING; 10116.ENSRNOP00000017239; -.
DR PhosphoSitePlus; Q4V7A0; -.
DR jPOST; Q4V7A0; -.
DR PaxDb; 10116-ENSRNOP00000017239; -.
DR Ensembl; ENSRNOT00055053578; ENSRNOP00055044302; ENSRNOG00055030856.
DR Ensembl; ENSRNOT00060030274; ENSRNOP00060024435; ENSRNOG00060017635.
DR Ensembl; ENSRNOT00065030370; ENSRNOP00065024147; ENSRNOG00065018103.
DR GeneID; 363064; -.
DR KEGG; rno:363064; -.
DR UCSC; RGD:1308228; rat.
DR AGR; RGD:1308228; -.
DR CTD; 80349; -.
DR RGD; 1308228; Skic8.
DR VEuPathDB; HostDB:ENSRNOG00000012803; -.
DR eggNOG; KOG4155; Eukaryota.
DR HOGENOM; CLU_000288_57_11_1; -.
DR InParanoid; Q4V7A0; -.
DR OrthoDB; 5667at2759; -.
DR PhylomeDB; Q4V7A0; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q4V7A0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000012803; Expressed in stomach and 20 other cell types or tissues.
DR ExpressionAtlas; Q4V7A0; baseline and differential.
DR Genevisible; Q4V7A0; RN.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0055087; C:Ski complex; ISS:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44090; WD REPEAT-CONTAINING PROTEIN 61; 1.
DR PANTHER; PTHR44090:SF1; WD REPEAT-CONTAINING PROTEIN 61; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; WD repeat; Wnt signaling pathway.
FT CHAIN 1..305
FT /note="Superkiller complex protein 8"
FT /id="PRO_0000425750"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..305
FT /note="Superkiller complex protein 8, N-terminally
FT processed"
FT /id="PRO_0000245853"
FT REPEAT 14..57
FT /note="WD 1"
FT REPEAT 62..101
FT /note="WD 2"
FT REPEAT 104..143
FT /note="WD 3"
FT REPEAT 146..187
FT /note="WD 4"
FT REPEAT 188..227
FT /note="WD 5"
FT REPEAT 230..269
FT /note="WD 6"
FT REPEAT 272..305
FT /note="WD 7"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZS3"
FT MOD_RES 2
FT /note="N-acetylthreonine; in WD repeat-containing protein
FT 61, N-terminally processed"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 305 AA; 33747 MW; 02EB895CA3C7E181 CRC64;
MTNQYSILFK QEQAHDDAIW SVAWETNKKE NIETVVTGSL DDLVKVWKWR DERLELQWSL
EGHQLGVVSV DISHTLPIAA SSSLDAHIRL WDLENGKQMK SIDAGPVDAW TLAFSPDSQH
LATGTHMGKV NIFGVESGKK EYSLDTRGKF ILSIAYSPDG KYLASGAIDG IINIFDIATG
KLLHTLEGHA MPIRSLTFSP DSQLLVTASD DGYIKIYDVQ HANLAGTLSG HASWVLNVAF
CPDDTHFVSS SSDKSVKVWD VGTRTCIHTF FDHQDQVWGV KYNGNGSKIV SVGDDQEIHV
YDCPI
//
